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UniProtKB/Swiss-Prot entry Q96QZ7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAGI1_HUMAN
Primary accession number Q96QZ7
Secondary accession numbers O00309 O43863 O75085 Q96QZ8 Q96QZ9
Integrated into Swiss-Prot on September 27, 2004
Sequence was last modified on September 27, 2004 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 67)
Name and origin of the protein
Protein name Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
Synonyms BAI1-associated protein 1
BAP-1
Membrane-associated guanylate kinase inverted 1
MAGI-1
Atrophin-1-interacting protein 3
AIP3
WW domain-containing protein 3
WWP3
Trinucleotide repeat-containing gene 19 protein
Gene name
Name: MAGI1
Synonyms: BAIAP1, BAP1, TNRC19
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND INTERACTION WITH BAI1.
TISSUE=Brain;
DOI=10.1006/bbrc.1998.8603; PubMed=9647739 [NCBI, ExPASy, EBI, Israel, Japan]
Shiratsuchi T., Futamura M., Oda K., Nishimori H., Nakamura Y., Tokino T.;
"Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1.";
Biochem. Biophys. Res. Commun. 247:597-604(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
DOI=10.1006/excr.2002.5475; PubMed=11969287 [NCBI, ExPASy, EBI, Israel, Japan]
Laura R.P., Ross S., Koeppen H., Lasky L.A.;
"MAGI-1: a widely expressed, alternatively spliced tight junction protein.";
Exp. Cell Res. 275:155-170(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 150-826 (ISOFORMS 1/3), TISSUE SPECIFICITY, AND INTERACTION WITH DRPLA.
DOI=10.1006/mcne.1998.0677; PubMed=9647693 [NCBI, ExPASy, EBI, Israel, Japan]
Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.;
"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.";
Mol. Cell. Neurosci. 11:149-160(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 152-371.
DOI=10.1074/jbc.272.23.14611; PubMed=9169421 [NCBI, ExPASy, EBI, Israel, Japan]
Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., Kay B.K., Fowlkes D.M.;
"Identification of novel human WW domain-containing proteins by cloning of ligand targets.";
J. Biol. Chem. 272:14611-14616(1997).
[5]
INTERACTION WITH SYNPO AND ACTN4.
DOI=10.1074/jbc.M203072200; PubMed=12042308 [NCBI, ExPASy, EBI, Israel, Japan]
Patrie K.M., Drescher A.J., Welihinda A., Mundel P., Margolis B.;
"Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1.";
J. Biol. Chem. 277:30183-30190(2002).
[6]
INTERACTION WITH IGSF5.
DOI=10.1128/MCB.23.12.4267-4282.2003; PubMed=12773569 [NCBI, ExPASy, EBI, Israel, Japan]
Hirabayashi S., Tajima M., Yao I., Nishimura W., Mori H., Hata Y.;
"JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1.";
Mol. Cell. Biol. 23:4267-4282(2003).
[7]
INTERACTION WITH FCHSD2.
DOI=10.1038/sj.onc.1206996; PubMed=14627983 [NCBI, ExPASy, EBI, Israel, Japan]
Ohno H., Hirabayashi S., Kansaku A., Yao I., Tajima M., Nishimura W., Ohnishi H., Mashima H., Fujita T., Omata M., Hata Y.;
"Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains.";
Oncogene 22:8422-8431(2003).
[8]
INTERACTION WITH ACCN3.
DOI=10.1074/jbc.M405874200; PubMed=15317815 [NCBI, ExPASy, EBI, Israel, Japan]
Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current.";
J. Biol. Chem. 279:46962-46968(2004).
[9]
INTERACTION WITH AMOT.
DOI=10.1074/jbc.M503915200; PubMed=16043488 [NCBI, ExPASy, EBI, Israel, Japan]
Bratt A., Birot O., Sinha I., Veitonmaeki N., Aase K., Ernkvist M., Holmgren L.;
"Angiomotin regulates endothelial cell-cell junctions and cell motility.";
J. Biol. Chem. 280:34859-34869(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB010894; BAA32002.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF401655; AAK94065.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF401656; AAK94066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF401654; AAK94064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80754; AAC04844.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U96115; AAC51326.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JE0209; JE0209.
RefSeq NP_001028229.1; -.
NP_004733.2; -.
NP_056335.1; -.
UniGene Hs.651939
3D structure databases
PDB
2Q9V; X-ray; 2.00 A; A=839-923.[ExPASy / RCSB / EBI]
2R4H; X-ray; 2.05 A; A/B/C=1146-1237.[ExPASy / RCSB / EBI]
2YSD; NMR; -; A=295-338.[ExPASy / RCSB / EBI]
2YSE; NMR; -; A=355-401.[ExPASy / RCSB / EBI]
3BPU; X-ray; 1.60 A; A=640-721.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2Q9V; -.
2R4H; -.
2YSD; -.
2YSE; -.
3BPU; -.
SMR Q96QZ7; 471-554, 994-1095.
ModBase Q96QZ7.
Protein-protein interaction databases
IntAct Q96QZ7; -.
PTM databases
PhosphoSite Q96QZ7; -.
Organism-specific databases
H-InvDB HIX0003428; -.
HGNC HGNC:946; MAGI1.
GeneLynx MAGI1; Homo sapiens.
GenAtlas MAGI1.
MIM 602625; gene. [NCBI / EBI]
PharmGKB PA25250; -.
GeneCards Q96QZ7.
Gene expression databases
ArrayExpress Q96QZ7; -.
CleanEx HS_BAP1; -.
HS_MAGI1; -.
GermOnline ENSG00000151276; Homo sapiens.
Ontologies
GO
GO:0005911; Cellular component: intercellular junction (traceable author statement from ProtInc).
GO:0008022; Molecular function: protein C-terminus binding (traceable author statement from ProtInc).
GO:0007155; Biological process: cell adhesion (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0006461; Biological process: protein complex assembly (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008144; Guanylate_kin.
IPR008145; Guanylt/Ca.
IPR001478; PDZ.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00625; Guanylate_kin; 1.
PF00595; PDZ; 5.
PF00397; WW; 2.
Pfam graphical view of domain structure.
SMART SM00072; GuKc; 1.
SM00228; PDZ; 6.
SM00456; WW; 2.
SMART graphical view of domain structure.
PROSITE PS00856; GUANYLATE_KINASE_1; 1.
PS50052; GUANYLATE_KINASE_2; 1.
PS50106; PDZ; 6.
PS01159; WW_DOMAIN_1; 2.
PS50020; WW_DOMAIN_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q96QZ7.
Genome annotation databases
Ensembl ENSG00000151276; Homo sapiens. [Contig view]
GeneID 9223; -.
KEGG hsa:9223; -.
Phylogenomic databases
HOGENOM Q96QZ7; -.
HOVERGEN Q96QZ7; -.
Other
LinkHub Q96QZ7; -.
SOURCE MAGI1; Homo sapiens.
ProtoNet Q96QZ7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell junction; Membrane; Nucleotide-binding; Phosphoprotein; Repeat; Tight junction.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1491  1491     Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1. PRO_0000094589
DOMAIN   17    105  89     PDZ 1. 
DOMAIN   96    287  192     Guanylate kinase-like. 
DOMAIN   300    333  34     WW 1. 
DOMAIN   359    392  34     WW 2. 
DOMAIN   472    554  83     PDZ 2. 
DOMAIN   643    721  79     PDZ 3. 
DOMAIN   813    895  83     PDZ 4. 
DOMAIN   970   1066  97     PDZ 5. 
DOMAIN   1124   1206  83     PDZ 6. 
NP_BIND   103    110  8     ATP (By similarity). 
REGION   970   1066  97     Interaction with FCHSD2. 
COMPBIAS   402    421  20     Poly-Gln. 
COMPBIAS   662    665  4     Poly-Gly. 
COMPBIAS   978    988  11     Poly-Gly. 
COMPBIAS   1341   1344  4     Poly-Ala. 
COMPBIAS   1398   1401  4     Poly-Arg. 
MOD_RES   866    866        Phosphotyrosine (By similarity). 
VAR_SEQ   806    834        PMSPSPASGLSKGEREREINSTNFGECPI -> L (in isoform 2, isoform 4, isoform 6 and isoform 7). VSP_011664
VAR_SEQ   1023   1099        GTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAV NGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNA -> VMQCQPPSWCHSALGGSKHCNSVMGAASLEVQIYSCNNP (in isoform 7). VSP_011665
VAR_SEQ   1027   1027        Missing (in isoform 2, isoform 4, isoform 5 and isoform 6). VSP_011666
VAR_SEQ   1028   1038        Missing (in isoform 4 and isoform 6). VSP_011667
VAR_SEQ   1039   1094        Missing (in isoform 4). VSP_011668
VAR_SEQ   1241   1288        DPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLH KSSPHGEK -> AMIPPNIAACMRNEKLGEACFYLMGHNQTTTPAATATAPP PVHKVFRK (in isoform 5). VSP_011669
VAR_SEQ   1241   1256        DPSSDRHGPATGPQGV -> GGSNYENIPSFPGMTP (in isoform 3 and isoform 4). VSP_011670
VAR_SEQ   1257   1288        Missing (in isoform 3 and isoform 4). VSP_011671
VAR_SEQ   1289   1491        Missing (in isoform 3, isoform 4 and isoform 5). VSP_011672
CONFLICT   775    775        A -> G (in Ref. 3; AAC04844). 
STRAND   304    310  7      
STRAND   316    320  5      
TURN   321    324  4      
STRAND   325    329  5      
TURN   331    333  3      
STRAND   363    369  7      
STRAND   371    373  3      
STRAND   375    379  5      
TURN   380    383  4      
STRAND   384    388  5      
HELIX   390    398  9      
STRAND   640    647  8      
STRAND   652    654  3      
STRAND   656    659  4      
STRAND   663    670  8      
STRAND   685    689  5      
HELIX   699    707  9      
STRAND   714    721  8      
STRAND   839    845  7      
STRAND   853    857  5      
STRAND   865    870  6      
HELIX   875    879  5      
STRAND   887    891  5      
HELIX   901    914  14      
STRAND   916    922  7      
STRAND   1150   1156  7      
STRAND   1163   1168  6      
HELIX   1170   1172  3      
STRAND   1176   1181  6      
HELIX   1186   1189  4      
STRAND   1198   1202  5      
HELIX   1212   1220  9      
TURN   1221   1224  4      
STRAND   1225   1231  7      
Sequence information
Length: 1491 AA [This is the length of the unprocessed precursor] Molecular weight: 164641 Da [This is the MW of the unprocessed precursor] CRC64: 1898962F733CEAC1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKVIQKKNH WTSRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAV EAAGLPGGGE 

        70         80         90        100        110        120 
GPRLGEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF 

       130        140        150        160        170        180 
QKGFPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYN FLTVKEFLDL EQSGTLLEVG 

       190        200        210        220        230        240 
TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHAENEE 

       250        260        270        280        290        300 
EDDVPEMNSS FTADSGEQEE HTLQETALPP VNSSIIAAPI TDPSQKFPQY LPLSAEDNLG 

       310        320        330        340        350        360 
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE 

       370        380        390        400        410        420 
LPAGWEKIED PVYGIYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQQQ QQQQQQQQQQ 

       430        440        450        460        470        480 
QTEEWTEDHS ALVPPVIPNH PPSNPEPARE VPLQGKPFFT RNPSELKGKF IHTKLRKSSR 

       490        500        510        520        530        540 
GFGFTVVGGD EPDEFLQIKS LVLDGPAALD GKMETGDVIV SVNDTCVLGH THAQVVKIFQ 

       550        560        570        580        590        600 
SIPIGASVDL ELCRGYPLPF DPDDPNTSLV TSVAILDKEP IIVNGQETYD SPASHSSKTG 

       610        620        630        640        650        660 
KVNGMKDARP SSPADVASNS SHGYPNDTVS LASSIATQPE LITVHIVKGP MGFGFTIADS 

       670        680        690        700        710        720 
PGGGGQRVKQ IVDSPRCRGL KEGDLIVEVN KKNVQALTHN QVVDMLVECP KGSEVTLLVQ 

       730        740        750        760        770        780 
RGGLPVPKKS PKSQPLERKD SQNSSQHSVS SHRSLHTASP SHSTQVLPEF PPAEAQAPDQ 

       790        800        810        820        830        840 
TDSSGQKKPD PFKIWAQSRS MYENRPMSPS PASGLSKGER EREINSTNFG ECPIPDYQEQ 

       850        860        870        880        890        900 
DIFLWRKETG FGFRILGGNE PGEPIYIGHI VPLGAADTDG RLRSGDELIC VDGTPVIGKS 

       910        920        930        940        950        960 
HQLVVQLMQQ AAKQGHVNLT VRRKVVFAVP KTENEVPSPA SSHHSSNQPA SLTEEKRTPQ 

       970        980        990       1000       1010       1020 
GSQNSLNTVS SGSGSTSGIG SGGGGGSGVV STVVQPYDVE IRRGENEGFG FVIVSSVSRP 

      1030       1040       1050       1060       1070       1080 
EAGTTFAGNA CVAMPHKIGR IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK 

      1090       1100       1110       1120       1130       1140 
EAGNTVTLRI IPGDESSNAT LLTNAEKIAT ITTTHTPSQQ GTQETRNTTK PKQESQFEFK 

      1150       1160       1170       1180       1190       1200 
APQATQEQDF YTVELERGAK GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL 

      1210       1220       1230       1240       1250       1260 
EINGETTKNM KHSRAIELIK NGGRRVRLFL KRGDGSVPEY DPSSDRHGPA TGPQGVPEVR 

      1270       1280       1290       1300       1310       1320 
AGPDRRQHPS LESSYPPDLH KSSPHGEKRA HARDPKGSRE YSRQPNEHHT WNGTSRKPDS 

      1330       1340       1350       1360       1370       1380 
GACRPKDRAP EGRRDAQAER AAAANGPKRR SPEKRREGTR SADNTLERRE KHEKRRDVSP 

      1390       1400       1410       1420       1430       1440 
ERRRERSPTR RRDGSPSRRR RSLERLLEQR RSPERRRGGS PERRAKSTDR RRARSPERRR 

      1450       1460       1470       1480       1490 
ERSLDKRNRE DRASHREREE ANLKQDAGRS SRHPPEQRRR PYKECSTDLS I 

Q96QZ7 in FASTA format

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